1j0x
From Proteopedia
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- | [[Image:1j0x.gif|left|200px]] | + | [[Image:1j0x.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)''' | + | {{Structure |
+ | |PDB= 1j0x |SIZE=350|CAPTION= <scene name='initialview01'>1j0x</scene>, resolution 2.4Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1J0X is a [ | + | 1J0X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J0X OCA]. |
==Reference== | ==Reference== | ||
- | Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase., Cowan-Jacob SW, Kaufmann M, Anselmo AN, Stark W, Grutter MG, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2218-27. Epub 2003, Nov 27. PMID:[http:// | + | Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase., Cowan-Jacob SW, Kaufmann M, Anselmo AN, Stark W, Grutter MG, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2218-27. Epub 2003, Nov 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14646080 14646080] |
[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]] | [[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:30 2008'' |
Revision as of 09:57, 20 March 2008
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, resolution 2.4Å | |||||||
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Ligands: | |||||||
Activity: | Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
Overview
The crystal structure of the tetrameric form of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) isolated from rabbit muscle was solved at 2.4 A resolution after careful dynamic light-scattering experiments to find a suitable buffer for crystallization trials. The refined model has a crystallographic R factor of 20.3%. Here, the first detailed model of a mammalian GAPDH is presented. The cofactor NAD(+) (nicotinamide adenine dinucleotide) is bound to two subunits of the tetrameric enzyme, which is consistent with the negative cooperativity of NAD(+) binding to this enzyme. The structure of rabbit-muscle GAPDH is of interest because it shares 91% sequence identity with the human enzyme; human GAPDH is a potential target for the development of anti-apoptotic drugs. In addition, differences in the cofactor-binding pocket compared with the homology-model structure of GAPDH from the malaria parasite Plasmodium falciparum could be exploited in order to develop novel selective and potential antimalaria drugs.
About this Structure
1J0X is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase., Cowan-Jacob SW, Kaufmann M, Anselmo AN, Stark W, Grutter MG, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2218-27. Epub 2003, Nov 27. PMID:14646080
Page seeded by OCA on Thu Mar 20 11:57:30 2008
Categories: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) | Oryctolagus cuniculus | Single protein | Anselmo, A N. | Cowan-Jacob, S W. | Grutter, M G. | Kaufmann, M. | Stark, W. | NAD | Apoptosis | Dehydrogenase | Mammalian gapdh | Negative cooperativity | Oxidoreductase | Rossmann fold